Author: Meytal Galilee; Akram Alian
Title: Multimerization of HIV-1 integrase hinges on conserved SH3-docking platforms Document date: 2018_4_16
ID: 4fuxbte0_17
Snippet: To gain further insights into the interactions made by NTD and CTD, and their interference with the catalytic activity of CCD, we assessed 3'-processing activity of truncated domain variants of HIV-1 IN. These truncation variants are not active in strand-transfer activity (24) (25) (26) , a result that we also validated here (not shown). We found that whereas the CCD (residues 56-209) and NTDCCD (residues 1-209) variants of HIV-1 IN are as compet.....
Document: To gain further insights into the interactions made by NTD and CTD, and their interference with the catalytic activity of CCD, we assessed 3'-processing activity of truncated domain variants of HIV-1 IN. These truncation variants are not active in strand-transfer activity (24) (25) (26) , a result that we also validated here (not shown). We found that whereas the CCD (residues 56-209) and NTDCCD (residues 1-209) variants of HIV-1 IN are as competent for the 3'-processing activity as the full-length enzyme, the CCDCTD (residues 56-288) is indeed defective ( Figure 4A ).
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